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7UEN

Genetic and structural basis of the human anti-alpha-galactosyl antibody response

Replaces:  6NUY
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron siteAustralian Synchrotron
BeamlineMX2
Temperature [K]100
Detector technologyPIXEL
Collection date2017-04-11
DetectorDECTRIS EIGER X 16M
Wavelength(s)0.9537
Spacegroup nameP 32 2 1
Unit cell lengths101.492, 101.492, 78.159
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution38.310 - 1.550
R-factor0.1298
Rwork0.128
R-free0.17470
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)generic Fab
RMSD bond length0.012
RMSD bond angle1.681
Data reduction softwareMOSFLM
Data scaling softwareAimless (0.5.32)
Phasing softwarePHASER (2.7.17)
Refinement softwareREFMAC (5.8.0267)
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]38.31038.3101.580
High resolution limit [Å]1.5508.4901.550
Rmerge0.0910.0571.757
Rmeas0.0930.0591.822
Rpim0.0210.0150.475
Total number of observations1276211741947508
Number of reflections676304673319
<I/σ(I)>17.245.42.5
Completeness [%]100.099.199.9
Redundancy18.915.914.3
CC(1/2)0.9990.9980.465
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8293Equal volumes of a protein (in 25 mM Tris (pH 8.0), 100 mM NaCl) and well solution (1.5 M NaH2PO4.H2O.K2HPO4, pH 8.0) were combined.

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PDB entries from 2024-05-15

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